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P53739

- FPK1_YEAST

UniProt

P53739 - FPK1_YEAST

Protein

Flippase kinase 1

Gene

FPK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Flippase activator that phosphorylates DFN1 and DFN2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Down-regulated by YKP1 phosphorylation. This effect is counteracted in the presence of mannosyl-inositolphosphorylceramide (MIPC).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei525 – 5251ATPPROSITE-ProRule annotation
    Active sitei621 – 6211Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi502 – 5109ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: SGD
    3. protein serine/threonine kinase activity Source: SGD

    GO - Biological processi

    1. lipid transport Source: UniProtKB-KW
    2. positive regulation of phospholipid translocation Source: SGD
    3. protein autophosphorylation Source: SGD
    4. protein phosphorylation Source: SGD
    5. response to pheromone Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33354-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flippase kinase 1 (EC:2.7.11.1)
    Gene namesi
    Name:FPK1
    Ordered Locus Names:YNR047W
    ORF Names:N3449
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNR047w.
    SGDiS000005330. FPK1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 893893Flippase kinase 1PRO_0000086154Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei140 – 1401Phosphoserine3 Publications
    Modified residuei144 – 1441Phosphoserine2 Publications
    Modified residuei171 – 1711Phosphoserine2 Publications
    Modified residuei175 – 1751Phosphoserine2 Publications
    Modified residuei185 – 1851Phosphoserine2 Publications
    Modified residuei300 – 3001Phosphoserine3 Publications
    Modified residuei414 – 4141Phosphoserine4 Publications
    Modified residuei462 – 4621Phosphoserine3 Publications

    Post-translational modificationi

    The N-terminal non-catalytic domain is phosphorylated by YPK1.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP53739.
    PaxDbiP53739.
    PRIDEiP53739.

    Expressioni

    Gene expression databases

    GenevestigatoriP53739.

    Interactioni

    Protein-protein interaction databases

    BioGridi35872. 80 interactions.
    DIPiDIP-6427N.
    IntActiP53739. 6 interactions.
    MINTiMINT-601192.
    STRINGi4932.YNR047W.

    Structurei

    3D structure databases

    ProteinModelPortaliP53739.
    SMRiP53739. Positions 420-854.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini496 – 777282Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini778 – 86184AGC-kinase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. KIN82 subfamily.PROSITE-ProRule annotation
    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063286.
    KOiK08286.
    OMAiGKIAYTP.
    OrthoDBiEOG7R2BT5.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53739-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGHHHEHEQ ERDHEQEHEH DSLQRPTTGS ERTRSISFSK LLTRSWKRNA    50
    SSSNNMSVSS VNLYSDPENS RESDHNNSGS EGQSSRFSKL KSMFQSGNSS 100
    KNASAHNSSQ SSLEGDSASS SSKLRYVKPM TSVANASPAS PPLSPTIPET 150
    DVLQTPKMVH IDQHEHEREH SNCGSPIMLS SSSFSPTVAR TGTGRRRSPS 200
    TPIMPSQNSN NSSSTSAIRP NNYRHHSGSQ GFSSNNPFRE RAGTVRSSNP 250
    YFAYQGLPTH AMSSHDLDEG FQPYANGSGI HFLSTPTSKT NSLTNTKNLS 300
    NLSLNEIKEN EEVQEFNNED FFFHDIPKDL SLKDTLNGSP SRGSSKSPTI 350
    TQTFPSIIVG FDNEYEEDNN NDKHDEKEEQ QTTTDNKTRN LSPTKQNGKA 400
    THPRIKIPLR RAASEPNGLQ LASATSPTSS SARKTSGSSN INDKIPGQSV 450
    PPPNSFFPQE PSPKISDFPE PRRSRRLRTK SFSNKFQDIM VGPQSFEKIR 500
    LLGQGDVGKV FLVREKKTNR VYALKVLSKD EMIKRNKIKR VLTEQEILAT 550
    SNHPFIVTLY HSFQSEDYLY LCMEYCMGGE FFRALQTRKT KCICEDDARF 600
    YASEVTAALE YLHLLGFIYR DLKPENILLH QSGHIMLSDF DLSIQAKDSK 650
    VPVVKGSAQS TLVDTKICSD GFRTNSFVGT EEYIAPEVIR GNGHTAAVDW 700
    WTLGILIYEM LFGFTPFKGD NTNETFTNIL KNEVSFPNNN EISRTCKDLI 750
    KKLLTKNESK RLGCKMGAAD VKKHPFFKKV QWSLLRNQEP PLIPVLSEDG 800
    YDFAKLSSNK KRQTSQDSHK HLDEQEKNMF EERVEYDDEV SEDDPFHDFN 850
    SMSLMEQDNN SMIYGNTNSY GKIAYTPNSN RSRSNSHRTF FKR 893
    Length:893
    Mass (Da):100,546
    Last modified:October 1, 1996 - v1
    Checksum:i26AF74EE956F80DB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z71662 Genomic DNA. Translation: CAA96328.1.
    BK006947 Genomic DNA. Translation: DAA10588.1.
    PIRiS63378.
    RefSeqiNP_014445.1. NM_001183224.1.

    Genome annotation databases

    EnsemblFungiiYNR047W; YNR047W; YNR047W.
    GeneIDi855783.
    KEGGisce:YNR047W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z71662 Genomic DNA. Translation: CAA96328.1 .
    BK006947 Genomic DNA. Translation: DAA10588.1 .
    PIRi S63378.
    RefSeqi NP_014445.1. NM_001183224.1.

    3D structure databases

    ProteinModelPortali P53739.
    SMRi P53739. Positions 420-854.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35872. 80 interactions.
    DIPi DIP-6427N.
    IntActi P53739. 6 interactions.
    MINTi MINT-601192.
    STRINGi 4932.YNR047W.

    Proteomic databases

    MaxQBi P53739.
    PaxDbi P53739.
    PRIDEi P53739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNR047W ; YNR047W ; YNR047W .
    GeneIDi 855783.
    KEGGi sce:YNR047W.

    Organism-specific databases

    CYGDi YNR047w.
    SGDi S000005330. FPK1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063286.
    KOi K08286.
    OMAi GKIAYTP.
    OrthoDBi EOG7R2BT5.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33354-MONOMER.

    Miscellaneous databases

    NextBioi 980256.
    PROi P53739.

    Gene expression databases

    Genevestigatori P53739.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR011993. PH_like_dom.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Identification of novel pheromone-response regulators through systematic overexpression of 120 protein kinases in yeast."
      Burchett S.A., Scott A., Errede B., Dohlman H.G.
      J. Biol. Chem. 276:26472-26478(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry."
      Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.
      Mol. Biol. Cell 19:1783-1797(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-185; SER-300; SER-414 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-144; SER-171; SER-175; SER-300; SER-414 AND SER-462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A protein kinase network regulates the function of aminophospholipid flippases."
      Roelants F.M., Baltz A.G., Trott A.E., Fereres S., Thorner J.
      Proc. Natl. Acad. Sci. U.S.A. 107:34-39(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION BY YPK1, ENZYME REGULATION.

    Entry informationi

    Entry nameiFPK1_YEAST
    AccessioniPrimary (citable) accession number: P53739
    Secondary accession number(s): D6W1M2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 752 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3